An Enzymatic Route to Selenazolines

• Published in: Chembiochem : a European journal of chemical biology Vol. 14; no. 5; pp. 564 - 567
• Main Authors: Koehnke, Jesko, Morawitz, Falk, Bent, Andrew F., Houssen, Wael E., Shirran, Sally L., Fuszard, Matthew A., Smellie, Iain A., Botting, Catherine H., Smith, Margaret C. M., Jaspars, Marcel, Naismith, James H.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 18.03.2013; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: Amino Acid Sequence; biochemistry; biosynthesis; Communications; Cysteine - chemistry; Cysteine - metabolism; Iodoacetamide - chemistry; Multienzyme Complexes - metabolism; Oxazoles - chemistry; Oxazoles - metabolism; patellamides; Peptides, Cyclic - biosynthesis; Peptides, Cyclic - chemistry; selenazolines; Selenium - chemistry; Selenium - metabolism; Selenocysteine - chemistry; Selenocysteine - metabolism; Serine - chemistry; Serine - metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thiazoles - chemistry; Thiazoles - metabolism; Threonine - chemistry; Threonine - metabolism
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.201300037

Ringing the changes: Selenazolines have applications in medicinal chemistry, but their synthesis is challenging. We report a new convenient and less toxic route to these heterocycles that starts from commercially available selenocysteine. The new route depends on a heterocyclase enzyme that creates oxazolines and thiazolines from serines/threonines and cysteines.